ArticleAntioxidants (Basel, Switzerland)2021
p53 Forms Redox-Dependent Protein-Protein Interactions through Cysteine 277.
Article in Antioxidants (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Integrated multi-PTM omics reveals key host pathways in human coronavirus 229E infection.Redox biology · 2026Article
- Nitration in cancer signaling.Redox biology · 2026Review
- Mutations in ammonia transporter RhBG that impair NHThe Journal of physiology · 2026Article
- Human P53 Expression in Yeast: Investigating Its Apoptotic Effects.Mini reviews in medicinal chemistry · 2026Review
- Deciphering the safeguarding role of cysteine residues in p53 against HCommunications chemistry · 2025Article
- Genomic landscape of a long-term surviving patient with metastatic cancer of the larynx: a case report.Frontiers in oncology · 2025Article
- Article
- Regulation of p53 Function by Formation of Non-Nuclear Heterologous Protein Complexes.Biomolecules · 2022Review
- Protein-protein interactions in plant antioxidant defense.Frontiers in plant science · 2022Review
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7 authors.
Funding
Abstract
Reversible cysteine oxidation plays an essential role in redox signaling by reversibly altering protein structure and function. Cysteine oxidation may lead to intra- and intermolecular disulfide formation, and the latter can drastically stabilize protein-protein interactions in a more oxidizing milieu. The activity of the tumor suppressor p53 is regulated at multiple levels, including various post-translational modification (PTM) and protein-protein interactions. In the past few decades, p53 has been shown to be a redox-sensitive protein, and undergoes reversible cysteine oxidation both in vitro and in vivo. It is not clear, however, whether p53 also forms intermolecular disulfides with interacting proteins and whether these redox-dependent interactions contribute to the regulation of p53. In the present study, by combining (co-)immunoprecipitation, quantitative mass spectrometry and Western blot we found that p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions. Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3θ and 53BP1. These interaction partners may play a role in fine-tuning p53 activity under oxidizing conditions.
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